Localized conformational changes trigger the pH-induced fibrillogenesis of an amyloidogenic λ light chain protein

Solvent conditions modulate the expression of the amyloidogenic potential of proteins. In this work the effect of pH on the fibrillogenic behavior and the conformational properties of 6aJL2, a model protein of the highly amyloidogenic variable light chain λ6a gene segment, was examined. Ordered aggr...

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Veröffentlicht in:	Biochimica et biophysica acta. General subjects 2018-07, Vol.1862 (7), p.1656-1666
Hauptverfasser:	Velázquez-López, Isabel, Valdés-García, Gilberto, Romero Romero, Sergio, Maya Martínez, Roberto, Leal-Cervantes, Ana I., Costas, Miguel, Sánchez-López, Rosana, Amero, Carlos, Pastor, Nina, Fernández Velasco, D. Alejandro
Format:	Artikel
Sprache:	eng
Schlagworte:	Acids - pharmacology AL amyloidogenesis Amyloid - chemistry Calorimetry, Differential Scanning Circular dichroism Differential scanning calorimetry Fluorescence Humans Hydrogen-Ion Concentration Immunoglobulin lambda-Chains - chemistry Immunoglobulin lambda-Chains - genetics Microscopy, Electron Models, Molecular Molecular dynamics Molecular Dynamics Simulation Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Protein Aggregates Protein Conformation - drug effects Protein Denaturation - drug effects Protein Folding Protein Stability Recombinant Proteins - chemistry Spectrometry, Fluorescence Urea - pharmacology
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Zusammenfassung:	Solvent conditions modulate the expression of the amyloidogenic potential of proteins. In this work the effect of pH on the fibrillogenic behavior and the conformational properties of 6aJL2, a model protein of the highly amyloidogenic variable light chain λ6a gene segment, was examined. Ordered aggregates showing the ultrastructural and spectroscopic properties observed in amyloid fibrils were formed in the 2.0–8.0 pH range. At pH
ISSN:	0304-4165 1872-8006
DOI:	10.1016/j.bbagen.2018.04.014